Superoxide dismutase: A comparison of rate constants

作者: Henry J. Forman , Irwin Fridovich

DOI: 10.1016/0003-9861(73)90636-X

关键词: Superoxide dismutaseXanthine oxidaseEnzymeReaction rate constantCytochrome cXanthineInorganic chemistryTetranitromethaneChemistryAqueous solution

摘要: O2−was introduced, at a constant rate, into buffered aqueous solutions, either by mechanical infusion of KO2, dissolved in tetrahydrofuran, or the situ action xanthine oxidase on plus oxygen. This O2− was allowed to react with ferricytochrome c tetranitromethane and formation reaction products, ferrocytochrome nitroform, respectively, monitored spectrophotometrically. That concentration Superoxide dismutase, which competed equally given levels cytochrome thus caused 50% inhibition rates accumulation determined. The rate for enzymatic dismutation copper zinc containing enzyme from bovine erythrocytes then calculated known constants found be 2 × 109m−1 sec−1 pH 7.8 8.5. obtained steady-state concentrations 10−8m → 10−13m range is full agreement results pulse radiolytic investigations were performed 10−5m range. second order independent 10−5 10−13m. Several distinct types dismutase have been described. These include mangano-enzymes Escherichia coli chicken liver mitochondria iron-enzyme E. coli. dismutations catalyzed these enzymes also investigated as function pH.

参考文章(9)
Bernard B. Keele, J.M. McCord, I. Fridovich, Superoxide Dismutase from Escherichia coli B: A NEW MANGANESE-CONTAINING ENZYME Journal of Biological Chemistry. ,vol. 245, pp. 6176- 6181 ,(1970) , 10.1016/S0021-9258(18)62675-4
Dina Klug, Joseph Rabani, Irwin Fridovich, A Direct Demonstration of the Catalytic Action of Superoxide Dismutase through the Use of Pulse Radiolysis Journal of Biological Chemistry. ,vol. 247, pp. 4839- 4842 ,(1972) , 10.1016/S0021-9258(19)44987-9
E.J. Land, A.J. Swallow, One-electron reactions in biochemical systems as studied by pulse radiolysis: V. Cytochrome c Archives of Biochemistry and Biophysics. ,vol. 145, pp. 365- 372 ,(1971) , 10.1016/0003-9861(71)90049-X
Joe M. McCord, Irwin Fridovich, Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN) Journal of Biological Chemistry. ,vol. 244, pp. 6049- 6055 ,(1969) , 10.1016/S0021-9258(18)63504-5
Joseph Rabani, William A. Mulac, Max S. Matheson, The Pulse Radiolysis of Aqueous Tetranitromethane.1 I. Rate Constants and the Extinction Coefficient of eaq-. II. Oxygenated Solutions The Journal of Physical Chemistry. ,vol. 69, pp. 53- 70 ,(1965) , 10.1021/J100885A011
D. J. Glover, S. G. Landsman, Spectrophotometric Method for Determination of Tetranitromethane in Solution and in Air. Analytical Chemistry. ,vol. 36, pp. 1690- 1691 ,(1964) , 10.1021/AC60214A072
Guiseppe Rotilio, Robert C Bray, E.Martin Fielden, A pulse radiolysis study of superoxide dismutase Biochimica et Biophysica Acta. ,vol. 268, pp. 605- 609 ,(1972) , 10.1016/0005-2744(72)90359-2
Charles Beauchamp, Irwin Fridovich, Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels☆ Analytical Biochemistry. ,vol. 44, pp. 276- 287 ,(1971) , 10.1016/0003-2697(71)90370-8
Gideon Czapski, Benon H. J. Bielski, THE FORMATION AND DECAY OF H2O3 AND HO2 IN ELECTRON-IRRADIATED AQUEOUS SOLUTIONS1 The Journal of Physical Chemistry. ,vol. 67, pp. 2180- 2184 ,(1963) , 10.1021/J100804A050